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O00086 (IMDH_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Gene names
Name:IMH3
Synonyms:IMD3
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Ref.1

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_03156

Cofactor

Potassium By similarity. HAMAP-Rule MF_03156

Enzyme regulation

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Potently inhibited by MPA. Ref.1

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_03156

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03156

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03156.

Developmental stage

Expressed at equal levels in the yeast or hyphal form. HAMAP-Rule MF_03156

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_03156
PRO_0000093685

Regions

Domain119 – 17860CBS 1
Domain182 – 23857CBS 2
Nucleotide binding276 – 2783NAD By similarity
Nucleotide binding326 – 3283NAD By similarity
Region366 – 3683IMP binding By similarity
Region389 – 3902IMP binding By similarity
Region413 – 4175IMP binding By similarity

Sites

Active site3331Thioimidate intermediate By similarity
Metal binding3281Potassium; via carbonyl oxygen By similarity
Metal binding3301Potassium; via carbonyl oxygen By similarity
Metal binding3331Potassium; via carbonyl oxygen By similarity
Metal binding5061Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5071Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5081Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3311IMP By similarity
Binding site4471IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
O00086 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 5F1E52611B1E1418

FASTA52156,239
        10         20         30         40         50         60 
MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP SSAVSLETKL 

        70         80         90        100        110        120 
TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC TSEEQAEMVR KVKKYENGFI 

       130        140        150        160        170        180 
NDPVVISPEV TVGEVKKMGE VLGFTSFPVT ENGKVGGKLV GIITSRDIQF HEDNKSPVSE 

       190        200        210        220        230        240 
VMTKDLVVGK KGISLTDGNE LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS 

       250        260        270        280        290        300 
FHSKQLLCGA AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ 

       310        320        330        340        350        360 
VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY GVTEFANKFG 

       370        380        390        400        410        420 
VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG DYFYRDGKRL KTYRGMGSID 

       430        440        450        460        470        480 
AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK 

       490        500        510        520 
SIDELRENVD NGEIRFEFRT ASAQFEGGVH GLHSYEKRLH N 

« Hide

References

[1]"Overexpression of a cloned IMP dehydrogenase gene of Candida albicans confers resistance to the specific inhibitor mycophenolic acid."
Koehler G.A., White T.C., Agabian N.
J. Bacteriol. 179:2331-2338(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION.
Strain: SS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85049 Genomic DNA. Translation: AAB51509.1.

3D structure databases

ProteinModelPortalO00086.
SMRO00086. Positions 9-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0000509.

2D gel databases

COMPLUYEAST-2DPAGEO00086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

CGDCAL0000509. IMH3.

Phylogenomic databases

eggNOGCOG0517.
PhylomeDBO00086.

Enzyme and pathway databases

UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_CANAX
AccessionPrimary (citable) accession number: O00086
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 11, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways